Number of the records: 1
Electro-detachment of kinesin motor domain from microtubule in silico
- 1.
SYSNO ASEP 0570259 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Electro-detachment of kinesin motor domain from microtubule in silico Author(s) Průša, Jiří (URE-Y)
Cifra, Michal (URE-Y) RID, ORCID, SAINumber of authors 2 Source Title Computational and Structural Biotechnology Journal. - : Elsevier - ISSN 2001-0370
Roč. 21, FEB 2023 (2023), s. 1349-1361Number of pages 13 s. Publication form Print - P Language eng - English Country NL - Netherlands Keywords Electric field ; Proteins ; Tubulin ; Microtubules ; Molecular dynamics simulation Subject RIV BH - Optics, Masers, Lasers OECD category Biophysics R&D Projects GX20-06873X GA ČR - Czech Science Foundation (CSF) Method of publishing Limited access Institutional support URE-Y - RVO:67985882 UT WOS 000933953200001 EID SCOPUS 85147798567 DOI 10.1016/j.csbj.2023.01.018 Annotation Kinesin is a motor protein essential in cellular functions, such as intracellular transport and cell-division, as well as for enabling nanoscopic transport in bio-nanotechnology. Therefore, for effective control of function for nanotechnological applications, it is important to be able to modify the function of kinesin. To cir-cumvent the limitations of chemical modifications, here we identify another potential approach for kinesin control: the use of electric forces. Using full-atom molecular dynamics simulations (247,358 atoms, total time 4.4 mu s), we demonstrate, for the first time, that the kinesin-1 motor domain can be detached from a microtubule by an intense electric field within the nanosecond timescale. We show that this effect is fielddirection dependent and field-strength dependent. A detailed analysis of the electric forces and the work carried out by electric field acting on the microtubule-kinesin system shows that it is the combined action of the electric field pulling on the-tubulin C-terminus and the electric-field-induced torque on the kinesin dipole moment that causes kinesin detachment from the microtubule. It is shown, for the first time in a mechanistic manner, that an electric field can dramatically affect molecular interactions in a heterologous functional protein assembly. Our results contribute to understanding of electromagnetic field-biomatter interactions on a molecular level, with potential biomedical and bio-nanotechnological applications for harnessing control of protein nanomotors.(c) 2023 The Author(s). Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology. This is an open access article under the CC BY-NC-ND license (http://creative-commons.org/licens es/by-nc-nd/4.0/) Workplace Institute of Radio Engineering and Electronics Contact Petr Vacek, vacek@ufe.cz, Tel.: 266 773 413, 266 773 438, 266 773 488 Year of Publishing 2024 Electronic address 10.1016/j.csbj.2023.01.018
Number of the records: 1